A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression

Cell. 1986 Jun 20;45(6):827-35. doi: 10.1016/0092-8674(86)90557-x.


Nuclear and cytoplasmic poly(A)-binding proteins have been purified from Saccharomyces cerevisiae, and antisera have been used to isolate a gene that encodes them. The gene occurs in a single copy on chromosome 5 and gives rise to a unique, unspliced 2.1 kb transcript. The nuclear protein appears to be derived from the cytoplasmic one by proteolytic cleavage into 53 and 17 kd polypeptides that remain associated during isolation. DNA sequence determination reveals four tandemly arrayed 90 amino acid regions of homology that probably represent poly(A)-binding domains. A 55 residue A-rich region upstream of the initiator methionine codon in the mRNA shows an affinity for poly(A)-binding protein comparable to that of poly(A)180-220, raising the possibility of feedback regulation of translation.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Carrier Proteins / genetics*
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism
  • Cell Nucleus / metabolism
  • Cytoplasm / metabolism
  • Gene Expression Regulation
  • Genes
  • Genes, Fungal*
  • Poly A / genetics*
  • Poly A / isolation & purification
  • Poly A / metabolism
  • Protein Biosynthesis
  • Protein Processing, Post-Translational
  • RNA, Fungal / genetics
  • RNA, Fungal / metabolism
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Repetitive Sequences, Nucleic Acid
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism


  • Carrier Proteins
  • RNA, Fungal
  • RNA, Messenger
  • Poly A

Associated data

  • GENBANK/M12780